Man-Ho Oh
  • Ph. D.
  • Man-Ho Oh
  • Plant Development Genetics
  • N11-307
  • Laboratory of Plant Developmental Genetics & Functional Proteomics (N11-308)
  • +82-42-821-5497

Academic Career

  • Ph.D., 1993, Seoul National University Seoul, Korea


  • Post-Doc., 1995-1999, North Carolina State University (Raleigh) NC, USA
  • Principal Investigator., 2001- 2004, TS Corporation R & D Center (Incheon), Korea
  • Senior Research Scientist., 2004-2013 USDA-ARS, University of Illinois (Urbana-Champaign) IL, USA
  • Associate Prof., 2013- Current, Chungnam National University

Research Interests

  • Receptor kinases signaling in plants

    Plants respond to developmental and environmental signals in part through membrane-localized receptor kinases that interact with other proteins to initiate a cascade of biochemical events resulting in altered cellular function. The genome of the model plant Arabidopsis thaliana encodes 223 Leucine-Rich Repeat Receptor-Like Kinases (LRR RLKs) with a structural organization similar to that of animal receptor kinases. Several of these plant LRR RLKs have been characterized in some detail and are known to play critical roles in regulating growth, morphogenesis, disease resistance, and responses to stress signals. Key to understanding LRR RLK action in specific signaling pathways is the identification of both membrane-bound and soluble protein partners.
    However, the functions and interacting protein networks of the vast majority of this large family of signal transduction molecules remain unknown. Besides a broad study of protein interactions, a selected group of LRR RLKs will be functionally characterized at a detailed biochemical level, including those LRR RLKs interacting with other proteins. The large number of Arabidopsis LRR RLKs suggests extensive possibilities for protein-protein interaction and thus, the diversification and amplification of signaling pathways. Using interdisciplinary approaches from plant genetics, biochemistry, mass spectrometry and proteomics, an extensive network of LRR RLK interacting proteins and signal transduction including brassinosteroid hormone and small peptides will be generated.

Selected Publication

  • Rameneni JJ, Lee Y, Dhandapani V, Yu X, Choi SR, Oh MH*, Lim YP*. 2015. Genomic and Post-Translational Modification Analysis of Leucine-Rich-Repeat Receptor-Like Kinases in Brassica rapa. PLoS One 2015 No20;10(11):e0142255. doi: 10.1371/journal.pone.0142255. eCollection 2015.
  • Oh MH*, Bender KW, Kim SY, Wu X, Lee S, Nou IS, Zielinski RE, Clouse SD, Huber SC. 2015. Functional analysis of the BRI1 receptor kinase by Thr-for-Ser substitution in a regulatory autophosphorylation site. Frontiers in Plant Science 10.3389/fpls.2015.00562.
  • Alberto P. Macho, Benjamin Schwessinger, Vardis Ntoukakis, Alexandre Brutus, Cécile Segonzac, Sonali Roy, Yasuhiro Kadota, Man-Ho Oh, Jan Sklenar, Paul Derbyshire, Rosa Lozano-Durán, Frederikke Gro Malinovsky, Jacqueline Monaghan, Frank L. Menke,1 Steven C. Huber, Sheng Yang He, Cyril Zipfel. 2014. A Bacterial Tyrosine Phosphatase Inhibits Plant Pattern Recognition Receptor Activation. Science 343: 1509-1512.
  • Oh, M.-H., Wang, X., Clouse, S. D. and Huber, S. C. 2012. Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1) receptor kinase by autophosphorylation within the Gly-rich loop. Proc. Natl. Acad. Sci. USA.109: 327-332.